Phosphate-activated glutaminase expression during tumor development

• Published in: FEBS letters Vol. 341; no. 1; pp. 39 - 42
• Main Authors: Aledo, Juan C., Segura, Juan A., Medina, Miguel A., Alonso, Francisco J., de Castro, Ignacio Núñez, Marquez, Javier
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 14.03.1994; Elsevier
• Subjects: Animals; Biological and medical sciences; Blotting, Northern; Carcinoma, Ehrlich Tumor - enzymology; Cell Division; Enzyme Activation; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; General aspects (metabolism, cell proliferation, established cell line...); Glutaminase - biosynthesis; Glutaminase expression; Medical sciences; Mice; Mitochondria - enzymology; PAG, phosphate-activated glutaminase; Phosphates - metabolism; SDS, sodium dodecyl sulphate; Tumor cell; Tumor Cells, Cultured; Tumor development; Tumor glutaminase; Tumors; SDS, sodium dodecyl sulphate; Tumor glutaminase; Glutaminase expression; PAG, phosphate-activated glutaminase; Tumor development; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; Enzyme; Rodentia; Malignant tumor; Gene expression; Cell transformation; Carcinogenesis; In vitro; Glutaminase; Vertebrata; Mitochondria; Mammalia; Enzymatic activity; Mouse; Animal; Hydrolases; Tumor cell
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)80236-X

Changes in phosphate-activated glutaminase activities determined in intact cells and isolated mitochondria have been followed during mouse Ehrlich ascites carcinoma development. Glutaminase activities parallel the levels of poly(A) + RNAs encoding for the mitochondrial phosphate activated glutaminase. During the exponential growth phase, maximum activity was observed and the relative abundance of glutaminase mRNA significantly increased with regard to the stationary growth phase. The presented results show that tumor phosphate-activated glutaminase is subject to long-term regulation by differential gene expression.